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Shape and oligomerization state of the cytoplasmic domain of the phototaxis transducer II from Natronobacterium pharaonis

, : Shape and oligomerization state of the cytoplasmic domain of the phototaxis transducer II from Natronobacterium pharaonis. Proceedings of the National Academy of Sciences of the United States of America 103(42): 15428-15433

Phototaxisal lows archaea to adjust flagellar motion in response to light. In the photophobic response of Natronobacterium pharaonis, light-activated sensory rhodopsin II causes conformational changes in the transducer II protein (pHtrll), initiating the twocomponent signaling system analogous to bacterial chemotaxis. pHtrII's cytoplasmic domain (pHtril-cyt) is homologous to the cytoplasmic domains of eubacterial chemotaxis receptors. Chemotaxis receptors require dimerization for activity and are in vivoorganized in large clusters. In this study we investigated the oligornerization and aggregation states of pHtrII-cyt by using chemical cross-linking, analytical gel-filtration chromatography, and small-angle neutron scattering. We show that pHtr11-cyt is monomeric in dilute buffers, but forms climers in 4 MI KCI, the physiological salt concentration for halophilic archaea. At high ammonium sulfate concentration, the protein forms higher-order aggregates. The monomeric protein has a rod-like shape, 202 angstrom in length and 14.4 angstrom in diameter; upon climerization the length increases to 248 angstrom and the diameter to 18.2 angstrom. These results suggest that under high salt concentration the shape and oligornerization state of pHtrII-cyt are comparable to those of chemotaxis receptors.


PMID: 17032755

DOI: 10.1073/pnas.0607201103

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